Embodiments disclosed herein relate to methods for reducing endotoxin levels in protein preparations, including unpurified, partially purified, and highly purified preparations. Endotoxins are lipopolysaccharides that originate from the cell walls of gram negative bacteria. They are ubiquitous contaminants of biological preparations, which poses a serious problem because they are broad-spectrum cytotoxins that can confound research results, give false results in diagnostic assays, and render intended therapeutic products unsafe for use. This makes it important to have effective materials and methods for their removal from the biological preparations in which they reside. Many such materials and methods have been developed. Known examples include the treatment of the preparation by anion exchange chromatography where in many cases the endotoxin binds more strongly than a desired protein in the sample (Chen, R., et al. Protein Expression and Purification 2009, 64, 76-81). Other known examples include hydroxyapatite chromatography (Gagnon, P., et al. BioProcess International 2006, 4, 50-60), immobilized metal affinity chromatography (Tan, L., et al. Journal of Chromatography A 2007, 1141, 226-234), affinity chromatography with immobilized histidine or polymixin B (Anspach, F., et al. Journal of Chromatography A 1995, 711, 81-92), affinity chromatography with immobilized polymixin B affinity chromatography with immobilized endotoxin-binding peptide derived recombinantly from Limulus amoebocytes (Ding, J., et al. Journal of Chromatography B 2001, 759, 237-246), differential extraction with the surfactant Triton X-113 (Cotten, M., et al. Gene Therapy 1994, 1, 239-246), and numerous proprietary commercial products and methods (Kang, Y., et al. Process Biochemistry 2000, 36, 85-92); Salema, V., et al. Pharmaceutical Technology Europe 2009, 21, 36-41); Clutterbuck, A., et al. Biopharm International 2007, 20, 24-31). All of these methods exploit the properties of the endotoxins' lipid-A and core polysaccharide regions, which together participate in strong hydrophobic interactions, metal affinity interactions, and/or strong electrostatic interactions with positively charged surfaces. A technique called void exclusion anion exchange has been described for IgG purification, that also reduces endotoxin content (Nian, R., et al. J. Chromatography A 1282 (2013) 127-132) it achieves broader utility than many previously known methods because it accommodates samples without requirement for their previous equilibration to particular chromatography conditions and its ability to achieve buffer exchange in conjunction with endotoxin removal. A technique employing supersaturated allantoin to remove endotoxin from protein preparations has been described that has the feature of tolerating a wide range of chemical conditions, including wide ranges of pH, wide ranges of salt concentration, and the presence of organic additives, including surfactants (Vagenende, V., et al. ACS. Appl. Mater. Interfaces 5 (2013) 4472-4478; Vagenende, V., et al. J. Chromatography A, 1310 (2013) 127-132).